Cytosolic sulfation of arylamines to form sulfamates is found to be mediate
d by sulfotransferases of three gene families (SULT1 to 3). Among them, a S
ULT3 form (ST3A1) showed a high selectivity for N-sulfation of N-substitute
d aryl and alicyclic compounds. SULT1 (phenol) and SULT2 (hydroxysteroid) s
ulfotransferases showed N-sulfating activities of carcinogenic heterocyclic
amines. For N-hydroxyarylamine O-sulfation, SULT1 forms showed high activi
ty. In rats, ST1C1 mediated the metabolic activation of N-hydroxyarylamines
. However, the related form. (ST1C2) in humans showed the negligible activi
ty. Instead, ST1A3 showed high metabolic activating abilities among human s
ulfotransferases. (C) 1999 Published by Elsevier Science Ireland Ltd. All r
ights reserved.